Browse Articles

Nanophotonic waveguide chip-to-world beam scanning

Interfacial configurational entropy tuning strategy enabling liquid alloys for efficient depolymerization of polyolefin waste

<i>Helicobacter pylori</i> Screen-and-Treat Programs for Gastric Cancer Prevention — IARC Working Group Report

Quantitative corrosion framework for anti-corrosive passivation design to extend calendar life in lithium metal batteries

Valuing Care Provided by Residents and Fellows — Toward Competency-Based Billing

Twist-induced orbital chirality in a photonic laser

Goals for Opioid Use Disorder Medications — Protection, Remission, and Recovery

Elucidating genetic backgrounds of myasthenia gravis in Japanese by genome-wide association studies and multi-omics analyses of thymoma

Dream Team

Strategic synthesis of FLPClusters toward catalysis

Vulvar Melanoma with Vaginal Extension

NAA40 and NAC cooperate in co-translational histone acetylation in humans

Abstract N-terminal acetylation is an abundant and predominantly co-translational modification in eukaryotes that profoundly affects folding, compartmentalization fidelity and turnover of target proteins. Unlike other N-acetyltransferases, human NatD is composed solely of the catalytic subunit NAA40 and exclusively modifies histone proteins H2A and H4. However, the molecular details of co-translational NAA40 activity have remained elusive. Here, we show biochemically and by cryo-EM how NAA40 activity is coordinated at the ribosomal peptide tunnel exit involving the NAC complex. We demonstrate that the NAA40-NAC interaction is required for efficient ribosome binding and histone acetylation. Furthermore, we provide insights on the potential coordination of methionine removal and subsequent NAA40-mediated acetylation by formation of a multienzyme complex on the ribosome involving METAP1. Therefore, our results illustrate the details of N-terminal histone acetylation by NAA40 and highlight the role of NAC as a general coordinator of nascent protein modification.

DB-OTO Gene Therapy for Inherited Deafness

Urban forestry for cooler cities faces three critical hurdles

Case 8-2026: A 57-Year-Old Woman with Chest Pain, Dyspnea, and Syncope

A large-scale coherent 4D imaging sensor

VHL synthetic lethality screens uncover CBF-β as a negative regulator of STING

Abstract Clear cell renal cell carcinoma (ccRCC) represents the most common form of kidney cancer and is typified by biallelic inactivation of the von Hippel-Lindau ( VHL ) tumour suppressor gene. Here, we undertake genome-wide CRISPR/Cas9 screening to reveal synthetic lethal interactors of VHL , and uncover that loss of Core Binding Factor β (CBF-β) causes cell death in VHL -null ccRCC cell lines and impairs tumour establishment and growth in vivo. This synthetic relationship is independent of the elevated activity of hypoxia inducible factors (HIFs) in VHL -null cells, but does involve the RUNX transcription factors that are known binding partners of CBF-β. Mechanistically, CBF-β loss leads to upregulation of type I interferon signalling, and we uncover a direct inhibitory role for CBF-β at the STING locus controlling Interferon Stimulated Gene expression. Targeting CBF-β in kidney cancer both selectively induces tumour cell lethality and promotes activation of type I interferon signalling.

The Cell and Gene Therapy Access Model — A Vision for Future Development

Mode hopping via nonlinear magnon-magnon coupling in a synthetic antiferromagnet

Current and Emerging Approaches to Evaluating Influenza Vaccine Performance